Linus Pauling Quotes

Life is a relationship among molecules and not a property of any molecule.

We may, I believe, anticipate that the chemist of the future who is interested in the structure of proteins, nucleic acids, polysaccharides, and other complex substances with high molecular weight will come to rely upon a new structural chemistry, involving precise geometrical relationships among the atoms in the molecules and the rigorous application of the new structural principles, and that great progress will be made, through this technique, in the attack, by chemical methods, on the problems of biology and medicine.

Even in the world of molecules the civilising influence of modest restraints is a cause for rejoicing.

Think about the whole world of biological complex sciences. We still don't understand the way a protein folds the way it does.

The study of the amino acid sequence around the disulphide bonds of the immunoglobulins was my own short-cut to the understanding of antibody diversity.

One day I discovered that one could get the barrier to internal rotation in ethane approximately right using this method. This was the beginning of my work on organic molecules.

The structure of many cellular macromolecules has been revealed at the atomic level using x-ray crystallography.

The detailed geometry of the coenzyme molecule as a whole is fascinating in its complexity.

In 1970, I had begun work on the basic pancreatic trypsin inhibitor which has later become the model compound for the development of protein NMR, molecular dynamics, and experimental folding studies in other laboratories.

If we introduce iron complexly into ooporphyrin, we obtain haemin.

Much of my work in biology has been driven by my early training in chemistry. When studying a new chemical compound, the first and most important thing is to determine its detailed molecular structure.

Molecular chemistry, the chemistry of the covalent bond, is concerned with uncovering and mastering the rules that govern the structures, properties and transformations of molecular species.

The blood pigment haemoglobin is a compound which can be split by diverse methods into its constituents, pigment and protein.

As can be seen even by this limited number of examples proteins carry out amazingly diverse functions.

This simple idea served to provide information on the geometrical shape of reacting molecules, and I was able to make the role of the frontier orbitals in chemical reactions more distinct through visualization, by drawing their diagrams.

The success in the determination of the high-resolution structures of ribosomal subunits and eventually the whole ribosome was the culmination of decades of effort.

X-Ray crystallography is nowadays an accurate and rapid method of determining conformation in the crystal lattice, which conformation usually corresponds to the preferred conformation in solution.

Few scientists acquainted with the chemistry of biological systems at the molecular level can avoid being inspired.

This led to the discovery that long chain fatty acids would remarkably stabilize serum albumin to heat denaturation, and would even reverse the denaturation by heat or concentrated urea solutions.

This work made me more and more interested in biological matter, and I decided that I really wanted to work on the X-ray analysis of biological molecules.

Even when they are saturated in the sense of the older theory of valence, the elementary atoms still possess sufficient chemical affinity to bind other seemingly also saturated atoms and groups of atoms, under generation of clearly defined atomic bonds.

Genes are effectively one-dimensional. If you write down the sequence of A, C, G and T, that's kind of what you need to know about that gene. But proteins are three-dimensional. They have to be because we are three-dimensional, and we're made of those proteins. Otherwise we'd all sort of be linear, unimaginably weird creatures.

The essential principles of the three-dimensional structure of organic molecules had been correctly formulated by the first Nobel laureate in Chemistry, Jacobus van't Hoff, as early as 1874.

It was Max Perutz who inspired me to go into structural biology when he gave a lecture at Harvard in 1963. As soon as I heard him talk, I decided that this is what I want to do.

When I started engineering proteins I didn't know how hard it would be.